PXD038235 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Proteomic analysis defines the interactome of telomerase in the protozoan parasite, Trypanosoma brucei |
Description | Telomeres are the nucleoprotein structures found at the ends of eukaryotic chromosomes. Conventional DNA polymerases are unable to fully replicate the telomeric end of the chromosome, which leads to a progressive loss of DNA after every cell division. This problem is solved by the ribonucleoprotein enzyme, telomerase. Proper maintenance of the telomeric end is critical for maintaining genome integrity in eukaryotes. The telomerase enzyme has two essential components: the telomerase RNA (TR), which provides the template required for telomeric DNA synthesis; and the catalytic protein telomerase reverse transcriptase (TERT) that catalyzes the extension of the telomeric DNA ends using the TR as a template. The action of telomerase prevents the progressive shortening of the telomeres after every cell division. The TR can form a large structural scaffold upon which many accessory proteins can bind to and form the complete telomerase holoenzyme in vivo. These accessory proteins are required for telomerase activity and regulation inside of cells. The interacting partners of the TERT protein have been extensively characterized in yeast, human, and Tetrahymena systems. These interactors have not been extensively studied in lower eukaryotes including clinically relevant human parasites, such as Trypanosoma brucei (T. brucei). To this end, we performed co-immunoprecipitation coupled to LC-MS/MS of TbTERT-FLAG-HA-HA from T. brucei cells using an anti-TbTERT antibody and protein G magnetic beads. An isotype matched IgG control was performed in tandem. Comparisons of enriched proteins in the IP vs. IgG control revealed previously known and novel interactors of TbTERT. These findings suggest potential mechanistic differences in telomere maintenance in T. brucei compared to higher eukaryotes. |
HostingRepository | PRIDE |
AnnounceDate | 2023-03-08 |
AnnouncementXML | Submission_2023-03-08_11:44:34.335.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | ShoulingXu |
SpeciesList | scientific name: Trypanosoma brucei; NCBI TaxID: 5691; |
ModificationList | iodoacetamide derivatized residue |
Instrument | Q Exactive HF |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2022-11-21 16:10:48 | ID requested | |
⏵ 1 | 2023-03-08 11:44:34 | announced | |
Publication List
Dataset with its publication pending |
Keyword List
submitter keyword: co-immunoprecipitation, telomerase, interaction partners,Trypanosoma brucei, telomerase RNA, LC-MS/MS |
Contact List
ShoulingXu |
contact affiliation | Carnegie Mass Spectrometry Facility |
contact email | sxu@ciw.edu |
lab head | |
ShoulingXu |
contact affiliation | Carnegie Institution at Stanford |
contact email | sxu@ciw.edu |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD038235
- Label: PRIDE project
- Name: Proteomic analysis defines the interactome of telomerase in the protozoan parasite, Trypanosoma brucei